Document Detail


Interfacial assembly of proteins and peptides: recent examples studied by neutron reflection.
MedLine Citation:
PMID:  19656822     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Through reviewing a number of recent neutron reflection studies of interfacial adsorption of peptides and proteins, this paper aims to demonstrate the significance of this technique in studying interfacial biomolecular processes by illustrating the typical structural details that can be derived. The review will start with the introduction of relevant theoretical background, followed by an outline of representative biomolecular systems that have recently been studied to indicate the technical strengths of neutron reflection.
Authors:
XiuBo Zhao; Fang Pan; Jian R Lu
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2009-08-05
Journal Detail:
Title:  Journal of the Royal Society, Interface / the Royal Society     Volume:  6 Suppl 5     ISSN:  1742-5662     ISO Abbreviation:  J R Soc Interface     Publication Date:  2009 Oct 
Date Detail:
Created Date:  2009-08-25     Completed Date:  2009-12-02     Revised Date:  2010-10-07    
Medline Journal Info:
Nlm Unique ID:  101217269     Medline TA:  J R Soc Interface     Country:  England    
Other Details:
Languages:  eng     Pagination:  S659-70     Citation Subset:  IM    
Affiliation:
Biological Physics Group, University of Manchester, Schuster Building, Oxford Road, Manchester M13 9PL, UK.
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MeSH Terms
Descriptor/Qualifier:
Binding Sites
Dimerization
Neutron Diffraction / methods*,  trends*
Peptides / chemistry*
Protein Binding
Protein Conformation
Proteins / chemistry*,  ultrastructure*
Grant Support
ID/Acronym/Agency:
//Biotechnology and Biological Sciences Research Council
Chemical
Reg. No./Substance:
0/Peptides; 0/Proteins

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